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Database: UniProt
Entry: M0ZK11_SOLTU
LinkDB: M0ZK11_SOLTU
Original site: M0ZK11_SOLTU 
ID   M0ZK11_SOLTU            Unreviewed;       444 AA.
AC   M0ZK11;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Aminoacylase {ECO:0000313|EnsemblPlants:PGSC0003DMT400002373};
GN   Name=102590216 {ECO:0000313|EnsemblPlants:PGSC0003DMT400002373};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400002373, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400002373}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400002373};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036696-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036696-
CC       2};
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DR   RefSeq; XP_006351890.1; XM_006351828.2.
DR   RefSeq; XP_006351891.1; XM_006351829.2.
DR   RefSeq; XP_006351892.1; XM_006351830.2.
DR   RefSeq; XP_015166174.1; XM_015310688.1.
DR   AlphaFoldDB; M0ZK11; -.
DR   STRING; 4113.M0ZK11; -.
DR   PaxDb; 4113-PGSC0003DMT400002373; -.
DR   EnsemblPlants; PGSC0003DMT400002373; PGSC0003DMT400002373; PGSC0003DMG400000909.
DR   GeneID; 102590216; -.
DR   Gramene; PGSC0003DMT400002373; PGSC0003DMT400002373; PGSC0003DMG400000909.
DR   KEGG; sot:102590216; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_5_0_1; -.
DR   InParanoid; M0ZK11; -.
DR   OMA; MDCVETI; -.
DR   OrthoDB; 158507at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004046; F:aminoacylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.150.900; -; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR   PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR   PANTHER; PTHR45892:SF3; PUTATIVE-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF036696; ACY-1; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036696-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR036696-2}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..444
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004010636"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ   SEQUENCE   444 AA;  50082 MW;  F9733D185591AA47 CRC64;
     MFDHLQRLPV LFFFLLLSLS FSESLHENKE SDTPISRFQG YLRINTAHPN PNYTDAINYL
     TNFANSIPNL HSKVIHLTPT SPLLLLTWPG SNPSLPSILF NSHLDSVPAE PDKWTHPPFS
     AHKTSDGRIF ARGAQDDKCI GMQYLEAIKA IQTSDSKFVP LRNVHILYVP EEEVGGFDGM
     GKFVELKEFE ELNLGFMMDE GQASPNDEFR VFYADRTPWH TVIKAVGTPG HGSKLYDNTA
     MENLMKSMEV ITKFRESMFD MVKAGLAANS EVISVNPVFL NAGTPSPTGF MMNMQPSEAE
     AGFDIRMPPT ADPELMRKII EEQWAPAWRN MTYKITEKGF LRDIMGRPLM TLASDSNPWW
     SVFNEAVTRA GGKLSKPEIL ASTTDARFMR RLGIPTFGFS PMKNTPILLH DHNENLKDTV
     YLEGIKVYEC IIKSLSSFEG SYEH
//
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